TYROSINASE AND HEMOCYANIN

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。血蓝蛋白(HC)是许多节肢动物和软体动物体内含铜的蓝色氧转运蛋白，可以被十二烷基硫酸钠或酶裂解激活，发挥酶促酚氧化酶的活性，从而模拟酪氨酸酶(Ty)或儿茶酚氧化酶(CO)的活性。我们的合作者提出，血蓝蛋白亚基的第一个结构域屏蔽了活性部位的入口，并在血蓝蛋白激活时倾斜、无序或裂解，为底物打开了一个入口。对于节肢动物的酪氨酸酶，这种机制应该是相同的，因为节肢动物的酪氨酸酶与血蓝蛋白具有相同的四元结构。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Hemocyanins (HC), the blue copper-containing oxygen-transporting proteins of many arthropods and molluscs can be activated by SDS or enzymatic cleavage to exert an enzymatic phenoloxidase activity; thereby mimicking the activity of tyrosinases (Ty) or catecholoxidases (CO). Our collaborators proposed that the first domain of a hemocyanin subunit shields the active site entrance and is tilted, disordered or cleaved upon activation in hemocyanin, opening an entrance for the substrates. This mechanism should be the same in the case of tyrosinase from arthropods, which have the same quaternary structure as hemocyanins.